chemerin neutralizing antibody Search Results


chemerin neutralizing antibody  (Bio-Techne corporation)
94
Bio-Techne corporation chemerin neutralizing antibody
Chemerin Neutralizing Antibody, supplied by Bio-Techne corporation, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/chemerin+neutralizing+antibody/pm37897505-113-14-20?v=Bio-Techne+corporation
Average 94 stars, based on 1 article reviews
chemerin neutralizing antibody - by Bioz Stars, 2026-07
94/100 stars
  Buy from Supplier
goat anti mouse chemerin  (R&D Systems)
93
R&D Systems goat anti mouse chemerin
Twenty-four hour conditioned media from 3T3-L1 ( A , C ) or BMSC ( B ) adipocytes treated with 20 ng mL −1 TNFα or an equivalent volume of the 0.1% BSA/PBS vehicle control were either incubated for 1 hour with 10 µg mL −1 of goat anti-mouse <t>chemerin</t> neutralization antibody or 10 µg mL −1 IgG control antibody ( A, B ), or separated by size using exclusion column with a 10 kDa molecular weight cutoff ( C ) prior to analysis by CMKLR1 bioassay. All bars represent the mean ± s.e.m. of 3 samples and are representative of 3 independent experiments. *P<0.05 compared to the goat IgG, 0.1% PBS/BSA control ( A, B ) or the 0.1% BSA/PBS control ( C ) and † P<0.05 compared to the within group goat IgG control ( A, B ) and the respective >10 kDa group ( C ), two-way ANOVA, followed by Bonferroni’s post hoc test.
Goat Anti Mouse Chemerin, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/chemerin+neutralizing+antibody/pmc03515524-83-50-53?v=R%26D+Systems
Average 93 stars, based on 1 article reviews
goat anti mouse chemerin - by Bioz Stars, 2026-07
93/100 stars
  Buy from Supplier
chemerin neutralising antibody  (R&D Systems)
94
R&D Systems chemerin neutralising antibody
A . Representative Western analysis of <t>chemerin</t> in media from ESCC CAMs and ATMs (left). Quantitative analysis by densitometry of chemerin abundance in media from ESCC CAMs and ATMs (n = 4 different pairs of myofibroblasts) (right). B . Concentration-dependent stimulation of MSC migration by chemerin in scratch wound migration assays (left) and Boyden chamber migration assays (right)(n = 3). C . Increased migration of MSCs in Boyden chambers in response to conditioned media (CM) from CAMs and their respective ATMs (left) (n = 4 different pairs of myofibroblasts). Stimulation of MSC migration by CAM-CM was inhibited by chemerin neutralizing antibody (Chem.Ab; 10 µg/ml) (center). MSC migration was decreased in response to CM from CAM1 and CAM4 cells transfected with chemerin siRNA#3 (right). Horizontal arrows, p<0.05, t- test (n = 3).
Chemerin Neutralising Antibody, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/chemerin+neutralizing+antibody/pmc04134237-38-23-27?v=R%26D+Systems
Average 94 stars, based on 1 article reviews
chemerin neutralising antibody - by Bioz Stars, 2026-07
94/100 stars
  Buy from Supplier

Image Search Results


Twenty-four hour conditioned media from 3T3-L1 ( A , C ) or BMSC ( B ) adipocytes treated with 20 ng mL −1 TNFα or an equivalent volume of the 0.1% BSA/PBS vehicle control were either incubated for 1 hour with 10 µg mL −1 of goat anti-mouse chemerin neutralization antibody or 10 µg mL −1 IgG control antibody ( A, B ), or separated by size using exclusion column with a 10 kDa molecular weight cutoff ( C ) prior to analysis by CMKLR1 bioassay. All bars represent the mean ± s.e.m. of 3 samples and are representative of 3 independent experiments. *P<0.05 compared to the goat IgG, 0.1% PBS/BSA control ( A, B ) or the 0.1% BSA/PBS control ( C ) and † P<0.05 compared to the within group goat IgG control ( A, B ) and the respective >10 kDa group ( C ), two-way ANOVA, followed by Bonferroni’s post hoc test.

Journal: PLoS ONE

Article Title: Elastase and Tryptase Govern TNFα-Mediated Production of Active Chemerin by Adipocytes

doi: 10.1371/journal.pone.0051072

Figure Lengend Snippet: Twenty-four hour conditioned media from 3T3-L1 ( A , C ) or BMSC ( B ) adipocytes treated with 20 ng mL −1 TNFα or an equivalent volume of the 0.1% BSA/PBS vehicle control were either incubated for 1 hour with 10 µg mL −1 of goat anti-mouse chemerin neutralization antibody or 10 µg mL −1 IgG control antibody ( A, B ), or separated by size using exclusion column with a 10 kDa molecular weight cutoff ( C ) prior to analysis by CMKLR1 bioassay. All bars represent the mean ± s.e.m. of 3 samples and are representative of 3 independent experiments. *P<0.05 compared to the goat IgG, 0.1% PBS/BSA control ( A, B ) or the 0.1% BSA/PBS control ( C ) and † P<0.05 compared to the within group goat IgG control ( A, B ) and the respective >10 kDa group ( C ), two-way ANOVA, followed by Bonferroni’s post hoc test.

Article Snippet: The nitrocellulose was subsequently washed with TBS for 5 min and incubated in 10 mL of Odyssey blocking buffer (LI-COR Biosciences, Lincoln, NE) containing 0.1% tween-20 (called western buffer) for 1 h. Once blocking was complete, the nitrocellulose was placed overnight in western buffer containing either a 1∶200 dilution of goat anti-mouse chemerin (R&D Systems), neutrophil elastase (M-18) or mast cell tryptase (G-12) (Santa Cruz, Biotechnology Inc.) or a 1∶50 dilution of goat anti-mouse tPA (C-16) or uPA (M-20) (Santa Cruz, Biotechnology Inc.).

Techniques: Control, Incubation, Neutralization, Molecular Weight, Bioassay

3T3-L1 adipocytes were treated for 24 hours with 20 ng mL −1 TNFα or 0.1% BSA/PBS vehicle control in combination with a 1∶200 dilution of a protease inhibitor cocktail (PIC) or its respective vehicle (1∶200 diluted DMSO) prior to analysis by CMKLR1 bioassay ( A, B ) or western blot ( C, D ). All bars represent the mean ± s.e.m. of 3 samples, and are representative of 3 independent experiments. Western blot analysis using an R&D anti-chemerin antibody is representative of 4 samples per group and 3 independent experiments. *P<0.05 compared to the 0.1% BSA/PBS, 1∶200 DMSO vehicle control, two-way ANOVA, followed by Bonferroni’s post hoc test.

Journal: PLoS ONE

Article Title: Elastase and Tryptase Govern TNFα-Mediated Production of Active Chemerin by Adipocytes

doi: 10.1371/journal.pone.0051072

Figure Lengend Snippet: 3T3-L1 adipocytes were treated for 24 hours with 20 ng mL −1 TNFα or 0.1% BSA/PBS vehicle control in combination with a 1∶200 dilution of a protease inhibitor cocktail (PIC) or its respective vehicle (1∶200 diluted DMSO) prior to analysis by CMKLR1 bioassay ( A, B ) or western blot ( C, D ). All bars represent the mean ± s.e.m. of 3 samples, and are representative of 3 independent experiments. Western blot analysis using an R&D anti-chemerin antibody is representative of 4 samples per group and 3 independent experiments. *P<0.05 compared to the 0.1% BSA/PBS, 1∶200 DMSO vehicle control, two-way ANOVA, followed by Bonferroni’s post hoc test.

Article Snippet: The nitrocellulose was subsequently washed with TBS for 5 min and incubated in 10 mL of Odyssey blocking buffer (LI-COR Biosciences, Lincoln, NE) containing 0.1% tween-20 (called western buffer) for 1 h. Once blocking was complete, the nitrocellulose was placed overnight in western buffer containing either a 1∶200 dilution of goat anti-mouse chemerin (R&D Systems), neutrophil elastase (M-18) or mast cell tryptase (G-12) (Santa Cruz, Biotechnology Inc.) or a 1∶50 dilution of goat anti-mouse tPA (C-16) or uPA (M-20) (Santa Cruz, Biotechnology Inc.).

Techniques: Control, Protease Inhibitor, Bioassay, Western Blot

3T3-L1 or BMSC adipocytes were treated with TNFα or 0.1% BSA/PBS vehicle control in combination with 0–30 µM of the serine protease inhibitor aprotinin or 0–100 µM of the cysteine protease inhibitor E-64 or an equivalent volume of their respective vehicle controls, water or 0.9% NaCl. The effect of these treatments on the apparent concentration of active chemerin in adipocyte media was measured by the CMKLR1 bioassay (A–C). The effect of these treatments on the immunodetectable levels of total chemerin in adipocyte media was measured by western blot and quantified by densitometry (D–F). For densitometry analysis, the dual vehicle treatment (i.e. 0.1% BSA/PBS with H 2 0 or 0.9% NaCl) served as the reference control and was assigned a value of 100%. All bars represent the mean ± s.e.m. of 3 samples and are representative of 3 independent experiments. Western blot using an R&D anti-chemerin antibody is representative of 4 samples per group and 3 independent experiments. * P<0.05 compared to the within group 0.1% BSA/PBS vehicle control, † P<0.05 compared to the TNFα/vehicle control groups, two-way ANOVA, followed by Bonferroni’s post hoc test (A–C).

Journal: PLoS ONE

Article Title: Elastase and Tryptase Govern TNFα-Mediated Production of Active Chemerin by Adipocytes

doi: 10.1371/journal.pone.0051072

Figure Lengend Snippet: 3T3-L1 or BMSC adipocytes were treated with TNFα or 0.1% BSA/PBS vehicle control in combination with 0–30 µM of the serine protease inhibitor aprotinin or 0–100 µM of the cysteine protease inhibitor E-64 or an equivalent volume of their respective vehicle controls, water or 0.9% NaCl. The effect of these treatments on the apparent concentration of active chemerin in adipocyte media was measured by the CMKLR1 bioassay (A–C). The effect of these treatments on the immunodetectable levels of total chemerin in adipocyte media was measured by western blot and quantified by densitometry (D–F). For densitometry analysis, the dual vehicle treatment (i.e. 0.1% BSA/PBS with H 2 0 or 0.9% NaCl) served as the reference control and was assigned a value of 100%. All bars represent the mean ± s.e.m. of 3 samples and are representative of 3 independent experiments. Western blot using an R&D anti-chemerin antibody is representative of 4 samples per group and 3 independent experiments. * P<0.05 compared to the within group 0.1% BSA/PBS vehicle control, † P<0.05 compared to the TNFα/vehicle control groups, two-way ANOVA, followed by Bonferroni’s post hoc test (A–C).

Article Snippet: The nitrocellulose was subsequently washed with TBS for 5 min and incubated in 10 mL of Odyssey blocking buffer (LI-COR Biosciences, Lincoln, NE) containing 0.1% tween-20 (called western buffer) for 1 h. Once blocking was complete, the nitrocellulose was placed overnight in western buffer containing either a 1∶200 dilution of goat anti-mouse chemerin (R&D Systems), neutrophil elastase (M-18) or mast cell tryptase (G-12) (Santa Cruz, Biotechnology Inc.) or a 1∶50 dilution of goat anti-mouse tPA (C-16) or uPA (M-20) (Santa Cruz, Biotechnology Inc.).

Techniques: Control, Protease Inhibitor, Concentration Assay, Bioassay, Western Blot

The concentrations of elastase, tryptase, and tPA in 24 hour conditioned media from 3T3-L1 and BMSC adipocytes treated with 20 ng mL −1 of TNFα or equivalent volume of 0.1% BSA/PBS vehicle control were measured by western blot analysis (A). The apparent concentration of active chemerin in 24 h conditioned media from 3T3-L1 adipocytes treated with 20 ng mL −1 of TNFα (B) or equivalent volume of 0.1% BSA/PBS (B, Inset) together with neutralizing antibodies for elastase and tryptase (alone or in combination) or IgG control was measured using the CMKLR1 bioassay. All bars represent the mean ± s.e.m. of 3 samples, and are representative of 2 independent experiments. Western blots are representative of 4 samples per group and 3 independent experiments. * P<0.05 compared to the TNFα/IgG or the 0.1% BSA/PBS/IgG (Inset) treated cells, † P<0.05 compared to the TNFα+anti-elastase or anti-tryptase treated cells, two-way ANOVA, followed by Bonferroni’s post hoc test.

Journal: PLoS ONE

Article Title: Elastase and Tryptase Govern TNFα-Mediated Production of Active Chemerin by Adipocytes

doi: 10.1371/journal.pone.0051072

Figure Lengend Snippet: The concentrations of elastase, tryptase, and tPA in 24 hour conditioned media from 3T3-L1 and BMSC adipocytes treated with 20 ng mL −1 of TNFα or equivalent volume of 0.1% BSA/PBS vehicle control were measured by western blot analysis (A). The apparent concentration of active chemerin in 24 h conditioned media from 3T3-L1 adipocytes treated with 20 ng mL −1 of TNFα (B) or equivalent volume of 0.1% BSA/PBS (B, Inset) together with neutralizing antibodies for elastase and tryptase (alone or in combination) or IgG control was measured using the CMKLR1 bioassay. All bars represent the mean ± s.e.m. of 3 samples, and are representative of 2 independent experiments. Western blots are representative of 4 samples per group and 3 independent experiments. * P<0.05 compared to the TNFα/IgG or the 0.1% BSA/PBS/IgG (Inset) treated cells, † P<0.05 compared to the TNFα+anti-elastase or anti-tryptase treated cells, two-way ANOVA, followed by Bonferroni’s post hoc test.

Article Snippet: The nitrocellulose was subsequently washed with TBS for 5 min and incubated in 10 mL of Odyssey blocking buffer (LI-COR Biosciences, Lincoln, NE) containing 0.1% tween-20 (called western buffer) for 1 h. Once blocking was complete, the nitrocellulose was placed overnight in western buffer containing either a 1∶200 dilution of goat anti-mouse chemerin (R&D Systems), neutrophil elastase (M-18) or mast cell tryptase (G-12) (Santa Cruz, Biotechnology Inc.) or a 1∶50 dilution of goat anti-mouse tPA (C-16) or uPA (M-20) (Santa Cruz, Biotechnology Inc.).

Techniques: Control, Western Blot, Concentration Assay, Bioassay

CMKLR1 bioassay and western blot analysis were used to identify the effect of bestatin, an inhibitor of aminopeptidases, alone and in combination with TNFα or a vehicle control on the apparent ( A ) and total ( B ) media chemerin concentration of 3T3-L1 adipocytes. All bars represent the mean ± s.e.m. of 3 samples and are representative of 3 independent experiments. Western blot using an R&D anti-chemerin antibody is representative of 4 samples per group and 3 independent experiments. † P<0.05 compared to the TNFα/vehicle control, two-way ANOVA followed by Bonferroni’s post hoc test ( A ).

Journal: PLoS ONE

Article Title: Elastase and Tryptase Govern TNFα-Mediated Production of Active Chemerin by Adipocytes

doi: 10.1371/journal.pone.0051072

Figure Lengend Snippet: CMKLR1 bioassay and western blot analysis were used to identify the effect of bestatin, an inhibitor of aminopeptidases, alone and in combination with TNFα or a vehicle control on the apparent ( A ) and total ( B ) media chemerin concentration of 3T3-L1 adipocytes. All bars represent the mean ± s.e.m. of 3 samples and are representative of 3 independent experiments. Western blot using an R&D anti-chemerin antibody is representative of 4 samples per group and 3 independent experiments. † P<0.05 compared to the TNFα/vehicle control, two-way ANOVA followed by Bonferroni’s post hoc test ( A ).

Article Snippet: The nitrocellulose was subsequently washed with TBS for 5 min and incubated in 10 mL of Odyssey blocking buffer (LI-COR Biosciences, Lincoln, NE) containing 0.1% tween-20 (called western buffer) for 1 h. Once blocking was complete, the nitrocellulose was placed overnight in western buffer containing either a 1∶200 dilution of goat anti-mouse chemerin (R&D Systems), neutrophil elastase (M-18) or mast cell tryptase (G-12) (Santa Cruz, Biotechnology Inc.) or a 1∶50 dilution of goat anti-mouse tPA (C-16) or uPA (M-20) (Santa Cruz, Biotechnology Inc.).

Techniques: Bioassay, Western Blot, Control, Concentration Assay

Our findings together support a model of adipocyte-derived proteolytic control of chemerin activity. Under basal conditions the activity of adipocyte-secreted chemerin (1) at CMKLR1 is determined by a precise balance between activation by serine and cysteine protease (2) and deactivation by aminopeptidases (3). Following treatment with TNFα, elevated secretion of chemerin (4) and production of elastase and tryptase (5) alter this balance resulting in increased concentration of a chemerin product(s) with high activity towards CMKLR1 (6).

Journal: PLoS ONE

Article Title: Elastase and Tryptase Govern TNFα-Mediated Production of Active Chemerin by Adipocytes

doi: 10.1371/journal.pone.0051072

Figure Lengend Snippet: Our findings together support a model of adipocyte-derived proteolytic control of chemerin activity. Under basal conditions the activity of adipocyte-secreted chemerin (1) at CMKLR1 is determined by a precise balance between activation by serine and cysteine protease (2) and deactivation by aminopeptidases (3). Following treatment with TNFα, elevated secretion of chemerin (4) and production of elastase and tryptase (5) alter this balance resulting in increased concentration of a chemerin product(s) with high activity towards CMKLR1 (6).

Article Snippet: The nitrocellulose was subsequently washed with TBS for 5 min and incubated in 10 mL of Odyssey blocking buffer (LI-COR Biosciences, Lincoln, NE) containing 0.1% tween-20 (called western buffer) for 1 h. Once blocking was complete, the nitrocellulose was placed overnight in western buffer containing either a 1∶200 dilution of goat anti-mouse chemerin (R&D Systems), neutrophil elastase (M-18) or mast cell tryptase (G-12) (Santa Cruz, Biotechnology Inc.) or a 1∶50 dilution of goat anti-mouse tPA (C-16) or uPA (M-20) (Santa Cruz, Biotechnology Inc.).

Techniques: Derivative Assay, Control, Activity Assay, Activation Assay, Concentration Assay

A . Representative Western analysis of chemerin in media from ESCC CAMs and ATMs (left). Quantitative analysis by densitometry of chemerin abundance in media from ESCC CAMs and ATMs (n = 4 different pairs of myofibroblasts) (right). B . Concentration-dependent stimulation of MSC migration by chemerin in scratch wound migration assays (left) and Boyden chamber migration assays (right)(n = 3). C . Increased migration of MSCs in Boyden chambers in response to conditioned media (CM) from CAMs and their respective ATMs (left) (n = 4 different pairs of myofibroblasts). Stimulation of MSC migration by CAM-CM was inhibited by chemerin neutralizing antibody (Chem.Ab; 10 µg/ml) (center). MSC migration was decreased in response to CM from CAM1 and CAM4 cells transfected with chemerin siRNA#3 (right). Horizontal arrows, p<0.05, t- test (n = 3).

Journal: PLoS ONE

Article Title: Increased Expression of Chemerin in Squamous Esophageal Cancer Myofibroblasts and Role in Recruitment of Mesenchymal Stromal Cells

doi: 10.1371/journal.pone.0104877

Figure Lengend Snippet: A . Representative Western analysis of chemerin in media from ESCC CAMs and ATMs (left). Quantitative analysis by densitometry of chemerin abundance in media from ESCC CAMs and ATMs (n = 4 different pairs of myofibroblasts) (right). B . Concentration-dependent stimulation of MSC migration by chemerin in scratch wound migration assays (left) and Boyden chamber migration assays (right)(n = 3). C . Increased migration of MSCs in Boyden chambers in response to conditioned media (CM) from CAMs and their respective ATMs (left) (n = 4 different pairs of myofibroblasts). Stimulation of MSC migration by CAM-CM was inhibited by chemerin neutralizing antibody (Chem.Ab; 10 µg/ml) (center). MSC migration was decreased in response to CM from CAM1 and CAM4 cells transfected with chemerin siRNA#3 (right). Horizontal arrows, p<0.05, t- test (n = 3).

Article Snippet: The effects were studied of phorbol 12-myristate 13-acetate (PMA), Ro320432, SB202190, SP600125, U0126, ISO-1 (Calbiochem, Darmstadt, Germany), LY294002 (New England labs, Hertfordshire, UK), chemerin neutralising antibody (MAb2325, R&D Systems), CCX-832 and CCX826 (ChemoCentryx, Mountain View, CA) .

Techniques: Western Blot, Concentration Assay, Migration, Transfection

A , Representative images from MSCs stained for vimentin (positive control) and chemR23 revealing knock-down (KD) after ChemR23 siRNA treatment (left). Knockdown of ChemR23, but not GPR1, inhibited MSC migration in response to chemerin (100 ng/ml)(center) and CAM-CM (right). B , Concentration-dependent inhibition of MSC migration in response to chemerin by the ChemR23 antagonist CCX832 (left) but not the control compound CCX826 (1 µM) (center). MSC migration in response to CAM-CM was inhibited similarly by chemerin neutralising antibody, and CCX832, but not CCX826 (1 µM)(right). C , Representative Western blot shows increased phosphorylation of p42/44, p38 and JNK-II kinases in MSCs treated with chemerin (100 ng/ml)(left). In Boyden chamber assays, chemerin-stimulated MSC migration was inhibited by the JNK-II inhibitor, SP600125 (50 µM), the p42/44 inhibitor, UO126 (10 µM), p38 inhibitor SB202190 (3 µM), and the PKC inhibitor Ro320432 (2 µM) but not by PIK3 inhibitor LY294002 (50 µM) (right). Horizontal arrows, p<0.05, ANOVA (n = 3 in each case).

Journal: PLoS ONE

Article Title: Increased Expression of Chemerin in Squamous Esophageal Cancer Myofibroblasts and Role in Recruitment of Mesenchymal Stromal Cells

doi: 10.1371/journal.pone.0104877

Figure Lengend Snippet: A , Representative images from MSCs stained for vimentin (positive control) and chemR23 revealing knock-down (KD) after ChemR23 siRNA treatment (left). Knockdown of ChemR23, but not GPR1, inhibited MSC migration in response to chemerin (100 ng/ml)(center) and CAM-CM (right). B , Concentration-dependent inhibition of MSC migration in response to chemerin by the ChemR23 antagonist CCX832 (left) but not the control compound CCX826 (1 µM) (center). MSC migration in response to CAM-CM was inhibited similarly by chemerin neutralising antibody, and CCX832, but not CCX826 (1 µM)(right). C , Representative Western blot shows increased phosphorylation of p42/44, p38 and JNK-II kinases in MSCs treated with chemerin (100 ng/ml)(left). In Boyden chamber assays, chemerin-stimulated MSC migration was inhibited by the JNK-II inhibitor, SP600125 (50 µM), the p42/44 inhibitor, UO126 (10 µM), p38 inhibitor SB202190 (3 µM), and the PKC inhibitor Ro320432 (2 µM) but not by PIK3 inhibitor LY294002 (50 µM) (right). Horizontal arrows, p<0.05, ANOVA (n = 3 in each case).

Article Snippet: The effects were studied of phorbol 12-myristate 13-acetate (PMA), Ro320432, SB202190, SP600125, U0126, ISO-1 (Calbiochem, Darmstadt, Germany), LY294002 (New England labs, Hertfordshire, UK), chemerin neutralising antibody (MAb2325, R&D Systems), CCX-832 and CCX826 (ChemoCentryx, Mountain View, CA) .

Techniques: Staining, Positive Control, Knockdown, Migration, Concentration Assay, Inhibition, Control, Western Blot, Phospho-proteomics

A , Representative Western blots showing MIF in MSC media (top left) and cell extracts (bottom left) treated with chemerin (Ch; 100 ng/ml) or IGF-II (100 ng/ml) for 15 min. ChemR23 knock-down decreased MIF release in response to chemerin (center). Chemerin-stimulated MSC migration was inhibited by MIF (200 ng/ml)(right). B , Suppression of MIF signaling with ISO-I (50 µM) further increased chemerin-stimulated migration. C , MIF knock-down in MSCs increased migration in response to 4 ng/ml, but not 20 ng/ml chemerin. Horizontal arrows, p<0.05, t- test (n = 3).

Journal: PLoS ONE

Article Title: Increased Expression of Chemerin in Squamous Esophageal Cancer Myofibroblasts and Role in Recruitment of Mesenchymal Stromal Cells

doi: 10.1371/journal.pone.0104877

Figure Lengend Snippet: A , Representative Western blots showing MIF in MSC media (top left) and cell extracts (bottom left) treated with chemerin (Ch; 100 ng/ml) or IGF-II (100 ng/ml) for 15 min. ChemR23 knock-down decreased MIF release in response to chemerin (center). Chemerin-stimulated MSC migration was inhibited by MIF (200 ng/ml)(right). B , Suppression of MIF signaling with ISO-I (50 µM) further increased chemerin-stimulated migration. C , MIF knock-down in MSCs increased migration in response to 4 ng/ml, but not 20 ng/ml chemerin. Horizontal arrows, p<0.05, t- test (n = 3).

Article Snippet: The effects were studied of phorbol 12-myristate 13-acetate (PMA), Ro320432, SB202190, SP600125, U0126, ISO-1 (Calbiochem, Darmstadt, Germany), LY294002 (New England labs, Hertfordshire, UK), chemerin neutralising antibody (MAb2325, R&D Systems), CCX-832 and CCX826 (ChemoCentryx, Mountain View, CA) .

Techniques: Western Blot, Knockdown, Migration

A , Representative fields from MSC transendothelial migration experiments showing migration of PKH67-labelled MSCs (left). CCX832 (1 µM) inhibited chemerin- (center) and CAM-CM stimulated MSC transendothelial migration but CCX826 (1 µM) had no effect (right). B , Chemerin, and IGF-II used as a positive control, promptly (30 min) stimulated proMMP2 abundance in media as detected by Western blot but had no effect on cellular proMMP2 abundance (left); chemerin significantly increased MMP-2 enzyme activity in MSC media detected by the selective substrate MCA-Pro-Leu-Ala-Nva-Dpa-Ala-Arg-NH 2 (right). C , Human recombinant MMP-2 (80 ng/ml) stimulated transendothelial migration and there was dose-dependent inhibition by an MMP-2 selective inhibitor (MMP-2 inhibitor I) (left). The MMP-2 inhibitor (60 µM) significantly inhibited chemerin-stimulated MSC transendothelial migration (centre). Horizontal arrows, p<0.05, t- test (n = 3).

Journal: PLoS ONE

Article Title: Increased Expression of Chemerin in Squamous Esophageal Cancer Myofibroblasts and Role in Recruitment of Mesenchymal Stromal Cells

doi: 10.1371/journal.pone.0104877

Figure Lengend Snippet: A , Representative fields from MSC transendothelial migration experiments showing migration of PKH67-labelled MSCs (left). CCX832 (1 µM) inhibited chemerin- (center) and CAM-CM stimulated MSC transendothelial migration but CCX826 (1 µM) had no effect (right). B , Chemerin, and IGF-II used as a positive control, promptly (30 min) stimulated proMMP2 abundance in media as detected by Western blot but had no effect on cellular proMMP2 abundance (left); chemerin significantly increased MMP-2 enzyme activity in MSC media detected by the selective substrate MCA-Pro-Leu-Ala-Nva-Dpa-Ala-Arg-NH 2 (right). C , Human recombinant MMP-2 (80 ng/ml) stimulated transendothelial migration and there was dose-dependent inhibition by an MMP-2 selective inhibitor (MMP-2 inhibitor I) (left). The MMP-2 inhibitor (60 µM) significantly inhibited chemerin-stimulated MSC transendothelial migration (centre). Horizontal arrows, p<0.05, t- test (n = 3).

Article Snippet: The effects were studied of phorbol 12-myristate 13-acetate (PMA), Ro320432, SB202190, SP600125, U0126, ISO-1 (Calbiochem, Darmstadt, Germany), LY294002 (New England labs, Hertfordshire, UK), chemerin neutralising antibody (MAb2325, R&D Systems), CCX-832 and CCX826 (ChemoCentryx, Mountain View, CA) .

Techniques: Migration, Positive Control, Western Blot, Activity Assay, Recombinant, Inhibition